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Thermus thermophilus amylomaltase at pH 5.6

Analyse Thermus thermophilus amylomaltase at pH 5.6 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2OWX
Type: protein
Length: 498 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 4-alpha-glucanotransferase
EC: 2.4.1.25
UniProt: Q72J82
Ligands: SUI
Pockets: 4 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	4-alpha-glucanotransferase (EC 2.4.1.25)	protein	498	46% helix, 13% strand	Q72J82

Ligands and binding sites

SUI · (3-amino-2,5-dioxo-1-pyrrolidinyl)acetic acid · ligand · chains A
MLI · Malonate ion · additive · chains A
GOL · Glycerol · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	120	0.79	0.97	31	empty
2	965	0.76	0.79	80	GOL
3	176	0.50	0.77	29	MLI
4	50	0.37	0.80	12	empty

Modifications

Observed in the structure: 2 covalent (covalent ligand).

Compared structures

2OWX · THERMUS THERMOPHILUS AMYLOMALTASE AT pH 5.6 · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q72J82
Elsewhere: RCSB PDB 2OWX · PDBe 2OWX · UniProt Q72J82

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